Chaperone domains convert prolyl isomerases into generic catalysts of protein folding

Proceedings of the National Academy of Sciences of the United States of America

Volumn 106, Issue 48, 2009, Pages 20282-20287

  Jakob, Roman P ^a   Zoldák, Gabriel ^a   Aumüller, Tobias ^b   Schmid, Franz X ^a  

^a UNIVERSITY OF BAYREUTH   (Germany)

^b MAX PLANCK RESEARCH UNIT FOR ENZYMOLOGY OF PROTEIN FOLDING   (Germany)

Author keywords

Folding catalysis; Folding helpers; Folding mechanism; SlyD; Trigger factor

Indexed keywords

CHAPERONE; ISOMERASE; PROLINE; PROLINE DERIVATIVE; TETRAPEPTIDE;

ARTICLE; CATALYST; CONTROLLED STUDY; ENZYME SPECIFICITY; ENZYME SUBSTRATE; PERFORMANCE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN VARIANT;

CATALYSIS; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HUMANS; KINETICS; MODELS, MOLECULAR; MOLECULAR CHAPERONES; PEPTIDYLPROLYL ISOMERASE; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; SPECTROMETRY, FLUORESCENCE; SUBSTRATE SPECIFICITY; TACROLIMUS BINDING PROTEIN 1A;

EID: 73949113446     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0909544106     Document Type: Article

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